Domain organization of the polymerizing mannosyltransferases involved in synthesis of the Escherichia coli O8 and O9a lipopolysaccharide O-antigens

32Citations
Citations of this article
46Readers
Mendeley users who have this article in their library.

This article is free to access.

Abstract

Background: Escherichia coli O8 and O9a polysaccharide repeat units are synthesized by serotype-specific multidomain (WbdA) mannosyltransferases. Results: The various WbdA domains are functional when expressed individually. Conclusion: The number of domains identified in each WbdA protein correlates with the different linkage types formed by the enzyme. Significance: Modular glycosyltransferases could be exploited for synthesis of precise glycoconjugates with medical and industrial applications. © 2012 by The American Society for Biochemistry and Molecular Biology, Inc.

Cite

CITATION STYLE

APA

Greenfield, L. K., Richards, M. R., Vinogradov, E., Wakarchuk, W. W., Lowary, T. L., & Whitfield, C. (2012). Domain organization of the polymerizing mannosyltransferases involved in synthesis of the Escherichia coli O8 and O9a lipopolysaccharide O-antigens. Journal of Biological Chemistry, 287(45), 38135–38149. https://doi.org/10.1074/jbc.M112.412577

Register to see more suggestions

Mendeley helps you to discover research relevant for your work.

Already have an account?

Save time finding and organizing research with Mendeley

Sign up for free